4CUK
Structure of Salmonella D-Lactate Dehydrogenase in complex with NADH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005829 | cellular_component | cytosol |
A | 0008720 | molecular_function | D-lactate dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0051287 | molecular_function | NAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005829 | cellular_component | cytosol |
B | 0008720 | molecular_function | D-lactate dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0051287 | molecular_function | NAD binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005829 | cellular_component | cytosol |
C | 0008720 | molecular_function | D-lactate dehydrogenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0051287 | molecular_function | NAD binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0005829 | cellular_component | cytosol |
D | 0008720 | molecular_function | D-lactate dehydrogenase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAI A 1331 |
Chain | Residue |
A | TYR100 |
A | ASP174 |
A | PRO175 |
A | TYR176 |
A | HIS204 |
A | CYS205 |
A | PRO206 |
A | ASN211 |
A | THR232 |
A | SER233 |
A | ASP258 |
A | VAL105 |
A | TYR260 |
A | HIS295 |
A | ALA297 |
A | HOH2057 |
A | HOH2075 |
A | HOH2104 |
A | ILE150 |
A | GLY151 |
A | THR152 |
A | GLY153 |
A | LYS154 |
A | ILE155 |
A | PHE173 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAI D 1331 |
Chain | Residue |
D | TYR100 |
D | VAL105 |
D | GLY151 |
D | GLY153 |
D | LYS154 |
D | ILE155 |
D | PHE173 |
D | ASP174 |
D | PRO175 |
D | TYR176 |
D | HIS204 |
D | CYS205 |
D | PRO206 |
D | ASN211 |
D | THR232 |
D | SER233 |
D | ASP258 |
D | TYR260 |
D | HIS295 |
D | ALA297 |
D | HOH2065 |
D | HOH2086 |
Functional Information from PROSITE/UniProt
site_id | PS00065 |
Number of Residues | 28 |
Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. AGVIGtGKIGvaalrilkgfgmr.LLaFD |
Chain | Residue | Details |
A | ALA147-ASP174 |
site_id | PS00670 |
Number of Residues | 23 |
Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LFaeSDVIsLHcPltpeNyhLlN |
Chain | Residue | Details |
A | LEU194-ASN216 |
site_id | PS00671 |
Number of Residues | 17 |
Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKnGvMIINtSRGaLID |
Chain | Residue | Details |
A | MET223-ASP239 |